2xrp - Revision history

OCA at 10:29, 9 May 2024

OCA — Thu, 09 May 2024 10:29:11 GMT

←Older revision		Revision as of 10:29, 9 May 2024
Line 22:		Line 22:
	==See Also==		==See Also==
	*[[Tubulin 3D Structures\|Tubulin 3D Structures]]		*[[Tubulin 3D Structures\|Tubulin 3D Structures]]
-	*[[Tubulin tyrosine ligase\|Tubulin tyrosine ligase]]	+	*[[Tubulin tyrosine ligase 3D structures\|Tubulin tyrosine ligase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:16, 18 October 2023

OCA — Wed, 18 Oct 2023 18:16:42 GMT

←Older revision		Revision as of 18:16, 18 October 2023
Line 3:		Line 3:
	<SX load='2xrp' size='340' side='right' viewer='molstar' caption='[[2xrp]], [[Resolution\|resolution]] 8.20Å' scene=''>		<SX load='2xrp' size='340' side='right' viewer='molstar' caption='[[2xrp]], [[Resolution\|resolution]] 8.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xrp]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XRP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xrp]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XRP FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>~~, ~~<scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 8.2Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[2wbe\|2wbe]], [[1z2b\|1z2b]], [[2bqq\|2bqq]], [[1sa1\|1sa1]], [[1mjd\|1mjd]], [[1jff\|1jff]], [[1tvk\|1tvk]], [[1sa0\|1sa0]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Tubulin_GTPase Tubulin GTPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.6 3.6.5.6]~~ </~~span~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrp OCA], [https://pdbe.org/2xrp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xrp RCSB], [https://www.ebi.ac.uk/pdbsum/2xrp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xrp ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrp OCA], [https://pdbe.org/2xrp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xrp RCSB], [https://www.ebi.ac.uk/pdbsum/2xrp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xrp ProSAT]</span></td></tr>
	</table>		</table>
-	== Disease ==
-	[[https://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Defects in DCX are the cause of lissencephaly X-linked type 1 (LISX1) [MIM:[https://omim.org/entry/300067 300067]]; also called X-LIS or LIS. LISX1 is a classic lissencephaly characterized by mental retardation and seizures that are more severe in male patients. Affected boys show an abnormally thick cortex with absent or severely reduced gyri. Clinical manifestations include feeding problems, abnormal muscular tone, seizures and severe to profound psychomotor retardation. Female patients display a less severe phenotype referred to as 'doublecortex'.<ref>PMID:9489699</ref> <ref>PMID:9489700</ref> <ref>PMID:9668176</ref> <ref>PMID:9817918</ref> <ref>PMID:11468322</ref> <ref>PMID:12552055</ref> Defects in DCX are the cause of subcortical band heterotopia X-linked (SBHX) [MIM:[https://omim.org/entry/300067 300067]]; also known as double cortex or subcortical laminar heterotopia (SCLH). SBHX is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal.<ref>PMID:9618162</ref> <ref>PMID:9989615</ref> <ref>PMID:10369164</ref> <ref>PMID:10441340</ref> <ref>PMID:10807542</ref> <ref>PMID:11601509</ref> <ref>PMID:11175293</ref> <ref>PMID:12390976</ref> Note=A chromosomal aberration involving DCX is found in lissencephaly. Translocation t(X;2)(q22.3;p25.1).
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). [[https://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May be part with PAFAH1B1/LIS-1 of overlapping, but distinct, signaling pathways that promote neuronal migration.<ref>PMID:22359282</ref> [[https://www.uniprot.org/uniprot/TBA1D_BOVIN TBA1D_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).	+	[https://www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_BOVIN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 31:		Line 28:
	</SX>		</SX>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Tubulin GTPase]]~~	+	[[Category: Amigues B]]
-	[[Category: Amigues, B]]	+	[[Category: Clare DK]]
-	[[Category: Clare~~, D K~~]]	+	[[Category: Fourniol FJ]]
-	[[Category: Fourniol~~, F J~~]]	+	[[Category: Francis F]]
-	[[Category: Francis, F]]	+	[[Category: Houdusse A]]
-	[[Category: Houdusse, A]]	+	[[Category: Moores CA]]
-	[[Category: Moores~~, C A~~]]	+	[[Category: Perderiset M]]
-	[[Category: Perderiset, M]]	+	[[Category: Sindelar CV]]
-	[[Category: Sindelar~~, C V~~]]	+	[[Category: Thomas G]]
-	[[Category: Thomas, G]]	+
-	~~[[Category: Structural protein~~]]	+

OCA at 10:38, 12 January 2022

OCA — Wed, 12 Jan 2022 10:38:32 GMT

←Older revision		Revision as of 10:38, 12 January 2022
Line 3:		Line 3:
	<SX load='2xrp' size='340' side='right' viewer='molstar' caption='[[2xrp]], [[Resolution\|resolution]] 8.20Å' scene=''>		<SX load='2xrp' size='340' side='right' viewer='molstar' caption='[[2xrp]], [[Resolution\|resolution]] 8.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xrp]] is a 9 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2XRP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xrp]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XRP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wbe\|2wbe]], [[1z2b\|1z2b]], [[2bqq\|2bqq]], [[1sa1\|1sa1]], [[1mjd\|1mjd]], [[1jff\|1jff]], [[1tvk\|1tvk]], [[1sa0\|1sa0]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wbe\|2wbe]], [[1z2b\|1z2b]], [[2bqq\|2bqq]], [[1sa1\|1sa1]], [[1mjd\|1mjd]], [[1jff\|1jff]], [[1tvk\|1tvk]], [[1sa0\|1sa0]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Tubulin_GTPase Tubulin GTPase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.6 3.6.5.6] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tubulin_GTPase Tubulin GTPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.6 3.6.5.6] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2xrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrp OCA], [~~http~~://pdbe.org/2xrp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2xrp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2xrp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2xrp ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrp OCA], [https://pdbe.org/2xrp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xrp RCSB], [https://www.ebi.ac.uk/pdbsum/2xrp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xrp ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Defects in DCX are the cause of lissencephaly X-linked type 1 (LISX1) [MIM:[~~http~~://omim.org/entry/300067 300067]]; also called X-LIS or LIS. LISX1 is a classic lissencephaly characterized by mental retardation and seizures that are more severe in male patients. Affected boys show an abnormally thick cortex with absent or severely reduced gyri. Clinical manifestations include feeding problems, abnormal muscular tone, seizures and severe to profound psychomotor retardation. Female patients display a less severe phenotype referred to as 'doublecortex'.<ref>PMID:9489699</ref> <ref>PMID:9489700</ref> <ref>PMID:9668176</ref> <ref>PMID:9817918</ref> <ref>PMID:11468322</ref> <ref>PMID:12552055</ref> Defects in DCX are the cause of subcortical band heterotopia X-linked (SBHX) [MIM:[~~http~~://omim.org/entry/300067 300067]]; also known as double cortex or subcortical laminar heterotopia (SCLH). SBHX is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal.<ref>PMID:9618162</ref> <ref>PMID:9989615</ref> <ref>PMID:10369164</ref> <ref>PMID:10441340</ref> <ref>PMID:10807542</ref> <ref>PMID:11601509</ref> <ref>PMID:11175293</ref> <ref>PMID:12390976</ref> Note=A chromosomal aberration involving DCX is found in lissencephaly. Translocation t(X;2)(q22.3;p25.1).	+	[[https://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Defects in DCX are the cause of lissencephaly X-linked type 1 (LISX1) [MIM:[https://omim.org/entry/300067 300067]]; also called X-LIS or LIS. LISX1 is a classic lissencephaly characterized by mental retardation and seizures that are more severe in male patients. Affected boys show an abnormally thick cortex with absent or severely reduced gyri. Clinical manifestations include feeding problems, abnormal muscular tone, seizures and severe to profound psychomotor retardation. Female patients display a less severe phenotype referred to as 'doublecortex'.<ref>PMID:9489699</ref> <ref>PMID:9489700</ref> <ref>PMID:9668176</ref> <ref>PMID:9817918</ref> <ref>PMID:11468322</ref> <ref>PMID:12552055</ref> Defects in DCX are the cause of subcortical band heterotopia X-linked (SBHX) [MIM:[https://omim.org/entry/300067 300067]]; also known as double cortex or subcortical laminar heterotopia (SCLH). SBHX is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal.<ref>PMID:9618162</ref> <ref>PMID:9989615</ref> <ref>PMID:10369164</ref> <ref>PMID:10441340</ref> <ref>PMID:10807542</ref> <ref>PMID:11601509</ref> <ref>PMID:11175293</ref> <ref>PMID:12390976</ref> Note=A chromosomal aberration involving DCX is found in lissencephaly. Translocation t(X;2)(q22.3;p25.1).
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). [[~~http~~://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May be part with PAFAH1B1/LIS-1 of overlapping, but distinct, signaling pathways that promote neuronal migration.<ref>PMID:22359282</ref> [[~~http~~://www.uniprot.org/uniprot/TBA1D_BOVIN TBA1D_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).	+	[[https://www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). [[https://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May be part with PAFAH1B1/LIS-1 of overlapping, but distinct, signaling pathways that promote neuronal migration.<ref>PMID:22359282</ref> [[https://www.uniprot.org/uniprot/TBA1D_BOVIN TBA1D_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	==See Also==		==See Also==
	*[[Tubulin 3D Structures\|Tubulin 3D Structures]]		*[[Tubulin 3D Structures\|Tubulin 3D Structures]]
		+	*[[Tubulin tyrosine ligase\|Tubulin tyrosine ligase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:08, 10 April 2020

OCA — Fri, 10 Apr 2020 17:08:25 GMT

←Older revision		Revision as of 17:08, 10 April 2020
Line 3:		Line 3:
	<SX load='2xrp' size='340' side='right' viewer='molstar' caption='[[2xrp]], [[Resolution\|resolution]] 8.20Å' scene=''>		<SX load='2xrp' size='340' side='right' viewer='molstar' caption='[[2xrp]], [[Resolution\|resolution]] 8.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xrp]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2XRP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xrp]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XRP FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wbe\|2wbe]], [[1z2b\|1z2b]], [[2bqq\|2bqq]], [[1sa1\|1sa1]], [[1mjd\|1mjd]], [[1jff\|1jff]], [[1tvk\|1tvk]], [[1sa0\|1sa0]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wbe\|2wbe]], [[1z2b\|1z2b]], [[2bqq\|2bqq]], [[1sa1\|1sa1]], [[1mjd\|1mjd]], [[1jff\|1jff]], [[1tvk\|1tvk]], [[1sa0\|1sa0]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tubulin_GTPase Tubulin GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.6 3.6.5.6] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tubulin_GTPase Tubulin GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.6 3.6.5.6] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2xrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrp OCA], [http://pdbe.org/2xrp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xrp RCSB], [http://www.ebi.ac.uk/pdbsum/2xrp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xrp ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2xrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrp OCA], [http://pdbe.org/2xrp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xrp RCSB], [http://www.ebi.ac.uk/pdbsum/2xrp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xrp ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 24:		Line 24:

	==See Also==		==See Also==
-	*[[Tubulin\|Tubulin]]	+	*[[Tubulin 3D Structures\|Tubulin 3D Structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:01, 6 March 2020

OCA — Fri, 06 Mar 2020 17:01:57 GMT

←Older revision		Revision as of 17:01, 6 March 2020
Line 1:		Line 1:

	==Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules==		==Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules==
-	<~~StructureSection~~ load='2xrp' size='340' side='right'caption='[[2xrp]], [[Resolution\|resolution]] 8.20Å' scene=''>	+	<SX load='2xrp' size='340' side='right' viewer='molstar' caption='[[2xrp]], [[Resolution\|resolution]] 8.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2xrp]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XRP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2xrp]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XRP FirstGlance]. <br>
Line 28:		Line 28:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Human]]		[[Category: Human]]

OCA at 07:31, 21 August 2019

OCA — Wed, 21 Aug 2019 07:31:26 GMT

←Older revision		Revision as of 07:31, 21 August 2019
Line 1:		Line 1:

	==Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules==		==Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules==
-	<StructureSection load='2xrp' size='340' side='right' caption='[[2xrp]], [[Resolution\|resolution]] 8.20Å' scene=''>	+	<StructureSection load='2xrp' size='340' side='right'caption='[[2xrp]], [[Resolution\|resolution]] 8.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2xrp]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XRP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2xrp]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XRP FirstGlance]. <br>
Line 22:		Line 22:
	</div>		</div>
	<div class="pdbe-citations 2xrp" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2xrp" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Tubulin\|Tubulin]]
	== References ==		== References ==
	<references/>		<references/>
Line 28:		Line 31:
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Tubulin GTPase]]		[[Category: Tubulin GTPase]]
	[[Category: Amigues, B]]		[[Category: Amigues, B]]

OCA at 21:38, 15 November 2017

OCA — Wed, 15 Nov 2017 21:38:29 GMT

←Older revision		Revision as of 21:38, 15 November 2017
Line 22:		Line 22:
	</div>		</div>
	<div class="pdbe-citations 2xrp" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2xrp" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Tubulin\|Tubulin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:24, 5 August 2016

OCA — Fri, 05 Aug 2016 12:24:35 GMT

←Older revision		Revision as of 12:24, 5 August 2016
Line 1:		Line 1:
		+
	==Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules==		==Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules==
	<StructureSection load='2xrp' size='340' side='right' caption='[[2xrp]], [[Resolution\|resolution]] 8.20Å' scene=''>		<StructureSection load='2xrp' size='340' side='right' caption='[[2xrp]], [[Resolution\|resolution]] 8.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xrp]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XRP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xrp]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XRP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wbe\|2wbe]], [[1z2b\|1z2b]], [[2bqq\|2bqq]], [[1sa1\|1sa1]], [[1mjd\|1mjd]], [[1jff\|1jff]], [[1tvk\|1tvk]], [[1sa0\|1sa0]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wbe\|2wbe]], [[1z2b\|1z2b]], [[2bqq\|2bqq]], [[1sa1\|1sa1]], [[1mjd\|1mjd]], [[1jff\|1jff]], [[1tvk\|1tvk]], [[1sa0\|1sa0]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tubulin_GTPase Tubulin GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.6 3.6.5.6] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tubulin_GTPase Tubulin GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.6 3.6.5.6] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xrp RCSB], [http://www.ebi.ac.uk/pdbsum/2xrp PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrp OCA], [http://pdbe.org/2xrp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xrp RCSB], [http://www.ebi.ac.uk/pdbsum/2xrp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xrp ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2xrp" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 28:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Tubulin GTPase]]		[[Category: Tubulin GTPase]]
	[[Category: Amigues, B]]		[[Category: Amigues, B]]

OCA at 13:55, 18 December 2014

OCA — Thu, 18 Dec 2014 13:55:33 GMT

←Older revision		Revision as of 13:55, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2xrp\| PDB=2xrp \| SCENE= }}~~	+	==Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules==
-	===Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules===	+	<StructureSection load='2xrp' size='340' side='right' caption='[[2xrp]], [[Resolution\|resolution]] 8.20Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20974813}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2xrp]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XRP FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wbe\|2wbe]], [[1z2b\|1z2b]], [[2bqq\|2bqq]], [[1sa1\|1sa1]], [[1mjd\|1mjd]], [[1jff\|1jff]], [[1tvk\|1tvk]], [[1sa0\|1sa0]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tubulin_GTPase Tubulin GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.6 3.6.5.6] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xrp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xrp RCSB], [http://www.ebi.ac.uk/pdbsum/2xrp PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Defects in DCX are the cause of lissencephaly X-linked type 1 (LISX1) [MIM:[http://omim.org/entry/300067 300067]]; also called X-LIS or LIS. LISX1 is a classic lissencephaly characterized by mental retardation and seizures that are more severe in male patients. Affected boys show an abnormally thick cortex with absent or severely reduced gyri. Clinical manifestations include feeding problems, abnormal muscular tone, seizures and severe to profound psychomotor retardation. Female patients display a less severe phenotype referred to as 'doublecortex'.<ref>PMID:9489699</ref> <ref>PMID:9489700</ref> <ref>PMID:9668176</ref> <ref>PMID:9817918</ref> <ref>PMID:11468322</ref> <ref>PMID:12552055</ref> Defects in DCX are the cause of subcortical band heterotopia X-linked (SBHX) [MIM:[http://omim.org/entry/300067 300067]]; also known as double cortex or subcortical laminar heterotopia (SCLH). SBHX is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal.<ref>PMID:9618162</ref> <ref>PMID:9989615</ref> <ref>PMID:10369164</ref> <ref>PMID:10441340</ref> <ref>PMID:10807542</ref> <ref>PMID:11601509</ref> <ref>PMID:11175293</ref> <ref>PMID:12390976</ref> Note=A chromosomal aberration involving DCX is found in lissencephaly. Translocation t(X;2)(q22.3;p25.1).
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). [[http://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May be part with PAFAH1B1/LIS-1 of overlapping, but distinct, signaling pathways that promote neuronal migration.<ref>PMID:22359282</ref> [[http://www.uniprot.org/uniprot/TBA1D_BOVIN TBA1D_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Microtubule-associated proteins (MAPs) are essential for regulating and organizing cellular microtubules (MTs). However, our mechanistic understanding of MAP function is limited by a lack of detailed structural information. Using cryo-electron microscopy and single particle algorithms, we solved the 8 A structure of doublecortin (DCX)-stabilized MTs. Because of DCX's unusual ability to specifically nucleate and stabilize 13-protofilament MTs, our reconstruction provides unprecedented insight into the structure of MTs with an in vivo architecture, and in the absence of a stabilizing drug. DCX specifically recognizes the corner of four tubulin dimers, a binding mode ideally suited to stabilizing both lateral and longitudinal lattice contacts. A striking consequence of this is that DCX does not bind the MT seam. DCX binding on the MT surface indirectly stabilizes conserved tubulin-tubulin lateral contacts in the MT lumen, operating independently of the nucleotide bound to tubulin. DCX's exquisite binding selectivity uncovers important insights into regulation of cellular MTs.

-	~~==Disease==~~	+	Template-free 13-protofilament microtubule-MAP assembly visualized at 8 A resolution.,Fourniol FJ, Sindelar CV, Amigues B, Clare DK, Thomas G, Perderiset M, Francis F, Houdusse A, Moores CA J Cell Biol. 2010 Nov 1;191(3):463-70. Epub 2010 Oct 25. PMID:20974813<ref>PMID:20974813</ref>
-	~~[[http://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Defects in DCX are the cause of lissencephaly X~~-~~linked type 1 (LISX1) [MIM:[http://omim.org/entry/300067 300067]]; also called X~~-~~LIS or LIS~~. LISX1 is a classic lissencephaly characterized by mental retardation and seizures that are more severe in male patients. Affected boys show an abnormally thick cortex with absent or severely reduced gyri. Clinical manifestations include feeding problems, ~~abnormal muscular tone~~, ~~seizures and severe to profound psychomotor retardation~~. Female patients display a less severe phenotype referred to as 'doublecortex'.<ref>PMID:9489699</ref><ref>PMID:9489700</ref><ref>PMID:9668176</ref><ref>PMID:9817918</ref><ref>PMID:11468322</ref><ref>PMID:12552055</ref> Defects in DCX are the cause of subcortical band heterotopia X-linked (~~SBHX~~) ~~[MIM~~:~~[http://omim~~.~~org/entry/300067 300067]]; also known as double cortex or subcortical laminar heterotopia (SCLH)~~. SBHX is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal.<ref>PMID:~~9618162</ref>~~<ref>PMID:~~9989615~~</ref><ref>PMID:10369164</ref><ref>PMID:10441340</ref><ref>PMID:10807542</ref><ref>PMID:11601509</ref><ref>PMID:11175293</ref><ref>PMID:12390976</ref> Note=A chromosomal aberration involving DCX is found in lissencephaly. Translocation t(X;2)(q22.3;p25.1).	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP~~, ~~one at an exchangeable site on the beta chain and one at~~ a ~~non-exchangeable site on the alpha chain (By similarity). [[http://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Microtubule-associated protein required for initial steps~~ of ~~neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with~~ the ~~putative neuronal protein kinase DCLK1 in binding to a target protein~~. ~~May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway~~. ~~May be part with PAFAH1B1/LIS-1~~ of ~~overlapping, but distinct, signaling pathways that promote neuronal migration~~.<~~ref~~>~~PMID:22359282~~</~~ref~~> [[http://www.uniprot.org/uniprot/TBA1D_BOVIN TBA1D_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).	+	</div>
-		+
-	~~==About this Structure==~~	+
-	[[2xrp]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRP OCA].	+

	==See Also==		==See Also==
	*[[Tubulin\|Tubulin]]		*[[Tubulin\|Tubulin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020974813</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Tubulin GTPase]]		[[Category: Tubulin GTPase]]
-	[[Category: Amigues, B.]]	+	[[Category: Amigues, B]]
-	[[Category: Clare, D K.]]	+	[[Category: Clare, D K]]
-	[[Category: Fourniol, F J.]]	+	[[Category: Fourniol, F J]]
-	[[Category: Francis, F.]]	+	[[Category: Francis, F]]
-	[[Category: Houdusse, A.]]	+	[[Category: Houdusse, A]]
-	[[Category: Moores, C A.]]	+	[[Category: Moores, C A]]
-	[[Category: Perderiset, M.]]	+	[[Category: Perderiset, M]]
-	[[Category: Sindelar, C V.]]	+	[[Category: Sindelar, C V]]
-	[[Category: Thomas, G.]]	+	[[Category: Thomas, G]]
	[[Category: Structural protein]]		[[Category: Structural protein]]

OCA at 22:09, 24 March 2013

OCA — Sun, 24 Mar 2013 22:09:46 GMT

←Older revision		Revision as of 22:09, 24 March 2013
Line 1:		Line 1:
-	[[Image:2xrp.png\|left\|200px]]
-
	{{STRUCTURE_2xrp\| PDB=2xrp \| SCENE= }}		{{STRUCTURE_2xrp\| PDB=2xrp \| SCENE= }}
-
	===Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules===		===Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into the 8-Angstrom Cryo-EM Map of Doublecortin- Stabilised Microtubules===
		+	{{ABSTRACT_PUBMED_20974813}}

-	~~{{ABSTRACT_PUBMED_20974813}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Defects in DCX are the cause of lissencephaly X-linked type 1 (LISX1) [MIM:[http://omim.org/entry/300067 300067]]; also called X-LIS or LIS. LISX1 is a classic lissencephaly characterized by mental retardation and seizures that are more severe in male patients. Affected boys show an abnormally thick cortex with absent or severely reduced gyri. Clinical manifestations include feeding problems, abnormal muscular tone, seizures and severe to profound psychomotor retardation. Female patients display a less severe phenotype referred to as 'doublecortex'.<ref>PMID:9489699</ref><ref>PMID:9489700</ref><ref>PMID:9668176</ref><ref>PMID:9817918</ref><ref>PMID:11468322</ref><ref>PMID:12552055</ref> Defects in DCX are the cause of subcortical band heterotopia X-linked (SBHX) [MIM:[http://omim.org/entry/300067 300067]]; also known as double cortex or subcortical laminar heterotopia (SCLH). SBHX is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal.<ref>PMID:9618162</ref><ref>PMID:9989615</ref><ref>PMID:10369164</ref><ref>PMID:10441340</ref><ref>PMID:10807542</ref><ref>PMID:11601509</ref><ref>PMID:11175293</ref><ref>PMID:12390976</ref> Note=A chromosomal aberration involving DCX is found in lissencephaly. Translocation t(X;2)(q22.3;p25.1).
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). [[http://www.uniprot.org/uniprot/DCX_HUMAN DCX_HUMAN]] Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May be part with PAFAH1B1/LIS-1 of overlapping, but distinct, signaling pathways that promote neuronal migration.<ref>PMID:22359282</ref> [[http://www.uniprot.org/uniprot/TBA1D_BOVIN TBA1D_BOVIN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:020974813</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020974813</ref><references group="xtra"/><references/>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]